PRS6B_MACFA
ID PRS6B_MACFA Reviewed; 418 AA.
AC Q4R7L3;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=26S proteasome regulatory subunit 6B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT3;
DE AltName: Full=Proteasome 26S subunit ATPase 4;
GN Name=PSMC4; ORFNames=QtsA-14940;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. PSMC4 belongs to the heterohexameric ring of AAA (ATPases
CC associated with diverse cellular activities) proteins that unfolds
CC ubiquitinated target proteins that are concurrently translocated into a
CC proteolytic chamber and degraded into peptides.
CC {ECO:0000250|UniProtKB:P43686}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits, a base containing 6 ATPases including PSMC4 and
CC few additional components. Interacts with NR1I3. Interacts with PAAF1.
CC Interacts with TRIM5. Interacts with ZFAND1 (By similarity).
CC {ECO:0000250|UniProtKB:P43686}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P43686}. Nucleus
CC {ECO:0000250|UniProtKB:P43686}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AB168803; BAE00909.1; -; mRNA.
DR RefSeq; NP_001271757.1; NM_001284828.1.
DR AlphaFoldDB; Q4R7L3; -.
DR SMR; Q4R7L3; -.
DR STRING; 9541.XP_005589273.1; -.
DR Ensembl; ENSMFAT00000010750; ENSMFAP00000036504; ENSMFAG00000034580.
DR GeneID; 101864886; -.
DR CTD; 5704; -.
DR VEuPathDB; HostDB:ENSMFAG00000034580; -.
DR eggNOG; KOG0727; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR OrthoDB; 571919at2759; -.
DR Proteomes; UP000233100; Chromosome 19.
DR Bgee; ENSMFAG00000034580; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:InterPro.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR035256; PSMC4.
DR PANTHER; PTHR23073:SF120; PTHR23073:SF120; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..418
FT /note="26S proteasome regulatory subunit 6B"
FT /id="PRO_0000249770"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P43686"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43686"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43686"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43686"
FT MOD_RES 397
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43686"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43686"
SQ SEQUENCE 418 AA; 47366 MW; 80F9523C61B88F0C CRC64;
MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE LEFLEVQEEY
IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT AIVGSTTGSN YYVRILSTID
RELLKPNASV ALHKHSNALV DVLPPEADSS IMMLTSDQKP DVMYADIGGM DIQKQEVREA
VELPLTHFEL YKQIGIDPPR GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL
GEGPRMVRDV FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS KMNLSEEVDL
EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE KAYKTVIKKD EQEHEFYK
